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The acidic patch is a negatively charged region of the nucleosome surface that serves as a conserved interaction hub for neighboring nucleosomes and chromatin binding proteins, often via salt bridges with arginine anchors [1]. The acidic patch plays a critical role in chromatin condensation and chromatin remodeling. Recombinant mononucleosomes containing acidic patch mutations can be used to study the biological functions of the acidic patch.
H2AE92K Recombinant Nucleosome with Linker DNA consists of 199 base pairs of DNA wrapped around an octamer core of histone proteins (two each of H2A, H2B, H3.1, and H4) to form a nucleosome, the basic repeating unit of chromatin. The 5’ biotin-TEG DNA consists of a core 147 bp 601 nucleosome assembly sequence flanked by 26 bp linker sequences as underlined below. Histone H2A contains a glutamate-to-lysine (E-to-K) substitution at position 92 (H2AE92K). H2AE92 resides in the H2A C-terminal extension and mediates chromatin binding with factors such as H4-N-terminal tail, LANA, RCC1, IL-33, Sir3, HMGN2, and SMARCA5/SNF2h, an ATPase subunit of the ISWI family of chromatin remodeling complexes. H2AE92K disrupts binding with SMARCB1/BAF47, a subunit of the SWI/SNF (BAF) family of chromatin remodeling complexes. These complexes serve a critical role in cell division, cell and tissue differentiation, and development, and SWI/SNF complex malfunction has been linked to over 20% of human cancers.
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EpiCypher
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EpiCypher
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EpiCypher
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EpiCypher
